Q5VYS8 · TUT7_HUMAN
- ProteinTerminal uridylyltransferase 7
- GeneTUT7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1495 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth (By similarity).
Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299).
Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (PubMed:25979828).
Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984).
In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing (PubMed:25979828, PubMed:28671666).
Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (PubMed:25979828).
Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165).
Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult (PubMed:18172165, PubMed:19703396, PubMed:22898984, PubMed:25480299, PubMed:25979828, PubMed:28671666).
TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (PubMed:30122351).
Catalytic activity
- RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
RNA(n) RHEA-COMP:14527 + CHEBI:46398 = CHEBI:33019 + RNA(n)-3'-uridine ribonucleotide RHEA-COMP:17348
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 1047-1050 | UTP (UniProtKB | ChEBI) | ||||
Sequence: SSKN | ||||||
Binding site | 1057-1060 | UTP (UniProtKB | ChEBI) | ||||
Sequence: SDLD | ||||||
Binding site | 1058 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 1060 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 1130 | UTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1152 | UTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1170-1174 | UTP (UniProtKB | ChEBI) | ||||
Sequence: SYAYT | ||||||
Binding site | 1286 | UTP (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Molecular Function | miRNA binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA uridylyltransferase activity | |
Molecular Function | uridylyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | miRNA metabolic process | |
Biological Process | oocyte maturation | |
Biological Process | polyuridylation-dependent mRNA catabolic process | |
Biological Process | pre-miRNA processing | |
Biological Process | retrotransposon silencing by mRNA destabilization | |
Biological Process | RNA 3' uridylation | |
Biological Process | RNA 3'-end processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTerminal uridylyltransferase 7
- EC number
- Short namesTUTase 7
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5VYS8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053753 | 40 | in dbSNP:rs2378695 | |||
Sequence: A → V | ||||||
Mutagenesis | 1060 | Abolishes inhibition of LIRE1 retrotransposition. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1097-1099 | Abolishes monouridylation activity. | ||||
Sequence: LPI → WPW |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,265 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000150957 | 1-1495 | UniProt | Terminal uridylyltransferase 7 | |||
Sequence: MGDTAKPYFVKRTKDRGTMDDDDFRRGHPQQDYLIIDDHAKGHGSKMEKGLQKKKITPGNYGNTPRKGPCAVSSNPYAFKNPIYSQPAWMNDSHKDQSKRWLSDEHTGNSDNWREFKPGPRIPVINRQRKDSFQENEDGYRWQDTRGCRTVRRLFHKDLTSLETTSEMEAGSPENKKQRSRPRKPRKTRNEENEQDGDLEGPVIDESVLSTKELLGLQQAEERLKRDCIDRLKRRPRNYPTAKYTCRLCDVLIESIAFAHKHIKEKRHKKNIKEKQEEELLTTLPPPTPSQINAVGIAIDKVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPAIMSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPPYVFALMAIFFLQQRKEPLLPVYLGSWIEGFSLSKLGNFNLQDIEKDVVIWEHTDSAAGDTGITKEEAPRETPIKRGQVSLILDVKHQPSVPVGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPKKRIAIEDPYSVKRNVARTLNSQPVFEYILHCLRTTYKYFALPHKITKSSLLKPLNAITCISEHSKEVINHHPDVQTKDDKLKNSVLAQGPGATSSAANTCKVQPLTLKETAESFGSPPKEEMGNEHISVHPENSDCIQADVNSDDYKGDKVYHPETGRKNEKEKVGRKGKHLLTVDQKRGEHVVCGSTRNNESESTLDLEGFQNPTAKECEGLATLDNKADLDGESTEGTEELEDSLNHFTHSVQGQTSEMIPSDEEEEDDEEEEEEEEPRLTINQREDEDGMANEDELDNTYTGSGDEDALSEEDDELGEAAKYEDVKECGKHVERALLVELNKISLKEENVCEEKNSPVDQSDFFYEFSKLIFTKGKSPTVVCSLCKREGHLKKDCPEDFKRIQLEPLPPLTPKFLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTINGLETAEGLDCVRTIEELARVLRKHSGLRNILPITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRLLSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPVIPVLQEIYKGEKKPEIFVDGWNIYFFDQIDELPTYWSECGKNTESVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWTSKYIVIEDPFDLNHNLGAGLSRKMTNFIMKAFINGRRVFGIPVKGFPKDYPSKMEYFFDPDVLTEGELAPNDRCCRICGKIGHFMKDCPMRRKVRRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLREKRCFICGREGHIKKECPQFKGSSGSLSSKYMTQGKASAKRTQQES | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 57 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 64 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 132 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 600 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 844 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 893 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 939 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 939 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 960 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1414 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-30 | Disordered | ||||
Sequence: MGDTAKPYFVKRTKDRGTMDDDDFRRGHPQ | ||||||
Compositional bias | 8-30 | Basic and acidic residues | ||||
Sequence: YFVKRTKDRGTMDDDDFRRGHPQ | ||||||
Region | 43-69 | Disordered | ||||
Sequence: HGSKMEKGLQKKKITPGNYGNTPRKGP | ||||||
Region | 89-140 | Disordered | ||||
Sequence: WMNDSHKDQSKRWLSDEHTGNSDNWREFKPGPRIPVINRQRKDSFQENEDGY | ||||||
Compositional bias | 93-112 | Basic and acidic residues | ||||
Sequence: SHKDQSKRWLSDEHTGNSDN | ||||||
Region | 162-205 | Disordered | ||||
Sequence: LETTSEMEAGSPENKKQRSRPRKPRKTRNEENEQDGDLEGPVID | ||||||
Zinc finger | 244-274 | Matrin-type | ||||
Sequence: YTCRLCDVLIESIAFAHKHIKEKRHKKNIKE | ||||||
Domain | 551-600 | PAP-associated 1 | ||||
Sequence: VGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPKKRIAIEDPYS | ||||||
Region | 734-757 | Disordered | ||||
Sequence: DDYKGDKVYHPETGRKNEKEKVGR | ||||||
Region | 831-898 | Disordered | ||||
Sequence: THSVQGQTSEMIPSDEEEEDDEEEEEEEEPRLTINQREDEDGMANEDELDNTYTGSGDEDALSEEDDE | ||||||
Compositional bias | 842-859 | Acidic residues | ||||
Sequence: IPSDEEEEDDEEEEEEEE | ||||||
Region | 951-1495 | Sufficient for monouridylation activity | ||||
Sequence: SKLIFTKGKSPTVVCSLCKREGHLKKDCPEDFKRIQLEPLPPLTPKFLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTINGLETAEGLDCVRTIEELARVLRKHSGLRNILPITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRLLSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPVIPVLQEIYKGEKKPEIFVDGWNIYFFDQIDELPTYWSECGKNTESVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWTSKYIVIEDPFDLNHNLGAGLSRKMTNFIMKAFINGRRVFGIPVKGFPKDYPSKMEYFFDPDVLTEGELAPNDRCCRICGKIGHFMKDCPMRRKVRRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLREKRCFICGREGHIKKECPQFKGSSGSLSSKYMTQGKASAKRTQQES | ||||||
Zinc finger | 963-980 | CCHC-type 1 | ||||
Sequence: VVCSLCKREGHLKKDCPE | ||||||
Domain | 1233-1286 | PAP-associated 2 | ||||
Sequence: SVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWTSKYIVIEDPFDLNH | ||||||
Zinc finger | 1345-1362 | CCHC-type 2 | ||||
Sequence: RCCRICGKIGHFMKDCPM | ||||||
Compositional bias | 1367-1408 | Basic and acidic residues | ||||
Sequence: RRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKED | ||||||
Region | 1367-1424 | Disordered | ||||
Sequence: RRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAA | ||||||
Zinc finger | 1451-1468 | CCHC-type 3 | ||||
Sequence: KRCFICGREGHIKKECPQ | ||||||
Region | 1466-1495 | Disordered | ||||
Sequence: CPQFKGSSGSLSSKYMTQGKASAKRTQQES | ||||||
Compositional bias | 1470-1495 | Polar residues | ||||
Sequence: KGSSGSLSSKYMTQGKASAKRTQQES |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q5VYS8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,495
- Mass (Da)171,229
- Last updated2004-12-07 v1
- Checksum1AAB0F5B37266FF9
Q5VYS8-2
- Name2
Q5VYS8-3
- Name3
Q5VYS8-4
- Name4
Q5VYS8-5
- Name5
Q5VYS8-6
- Name6
- Differences from canonical
- 1157-1194: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5VYS9 | Q5VYS9_HUMAN | TUT7 | 168 | ||
Q5VYT0 | Q5VYT0_HUMAN | TUT7 | 124 | ||
X6R3Q3 | X6R3Q3_HUMAN | TUT7 | 784 | ||
A0A0C4DFW3 | A0A0C4DFW3_HUMAN | TUT7 | 395 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-30 | Basic and acidic residues | ||||
Sequence: YFVKRTKDRGTMDDDDFRRGHPQ | ||||||
Compositional bias | 93-112 | Basic and acidic residues | ||||
Sequence: SHKDQSKRWLSDEHTGNSDN | ||||||
Sequence conflict | 157 | in Ref. 4; BAB70951 | ||||
Sequence: K → R | ||||||
Sequence conflict | 316 | in Ref. 1; CAE46038 | ||||
Sequence: R → T | ||||||
Alternative sequence | VSP_013832 | 363-486 | in isoform 4 | |||
Sequence: MSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPPYVFALMAIFFLQQRKEPLLPVYLGSWI → I | ||||||
Alternative sequence | VSP_013833 | 403-412 | in isoform 5 | |||
Sequence: SGLLCKVSAG → RSHFFKLFIY | ||||||
Alternative sequence | VSP_013834 | 413-1495 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 514 | in Ref. 1; CAE46038 | ||||
Sequence: S → N | ||||||
Alternative sequence | VSP_013835 | 538-544 | in isoform 3 | |||
Sequence: SLILDVK → VSSLLCR | ||||||
Alternative sequence | VSP_013836 | 545-1495 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_013837 | 597-615 | in isoform 2 | |||
Sequence: DPYSVKRNVARTLNSQPVF → GISKCLSYSPPLFFLKVPV | ||||||
Alternative sequence | VSP_013838 | 616-1495 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 842-859 | Acidic residues | ||||
Sequence: IPSDEEEEDDEEEEEEEE | ||||||
Sequence conflict | 900 | in Ref. 1; CAI45944 | ||||
Sequence: G → V | ||||||
Sequence conflict | 937 | in Ref. 1; CAI45944/CAH56219 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_013839 | 960-1072 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 1104 | in Ref. 1; CAH56219 | ||||
Sequence: V → M | ||||||
Alternative sequence | VSP_013840 | 1157-1194 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 1319 | in Ref. 1; CAH56219 | ||||
Sequence: P → S | ||||||
Compositional bias | 1367-1408 | Basic and acidic residues | ||||
Sequence: RRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKED | ||||||
Compositional bias | 1470-1495 | Polar residues | ||||
Sequence: KGSSGSLSSKYMTQGKASAKRTQQES | ||||||
Sequence conflict | 1474 | in Ref. 1; CAI45944 | ||||
Sequence: G → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL832026 EMBL· GenBank· DDBJ | CAH56219.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832193 EMBL· GenBank· DDBJ | CAH56214.1 EMBL· GenBank· DDBJ | mRNA | ||
BX641077 EMBL· GenBank· DDBJ | CAE46038.1 EMBL· GenBank· DDBJ | mRNA | ||
CR933643 EMBL· GenBank· DDBJ | CAI45944.1 EMBL· GenBank· DDBJ | mRNA | ||
CR933644 EMBL· GenBank· DDBJ | CAI45945.1 EMBL· GenBank· DDBJ | mRNA | ||
CR936608 EMBL· GenBank· DDBJ | CAI56753.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137849 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL353678 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC032456 EMBL· GenBank· DDBJ | AAH32456.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023471 EMBL· GenBank· DDBJ | BAB14584.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK055546 EMBL· GenBank· DDBJ | BAB70951.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055948 EMBL· GenBank· DDBJ | BAB71052.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB051498 EMBL· GenBank· DDBJ | BAB21802.1 EMBL· GenBank· DDBJ | mRNA |